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Q9U8B8 (DYR_HELVI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrofolate reductase

EC=1.5.1.3
Gene names
Name:DHFR
OrganismHeliothis virescens (Tobacco budworm moth)
Taxonomic identifier7102 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaNoctuidaeHeliothinaeHeliothis

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis By similarity.

Catalytic activity

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH. UniProtKB P28019

Enzyme regulation

Activated by dithiothreitol and p-chloromercuribenzoate. Inhibited by trimethoprim, methotrexate, sodium tetrathionate and hydroxymercuribenzoate. Ref.1

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.

Sequence similarities

Belongs to the dihydrofolate reductase family. UniProtKB P28019

Contains 1 DHFR (dihydrofolate reductase) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 185185Dihydrofolate reductase
PRO_0000186371

Regions

Domain5 – 184180DHFR
Nucleotide binding17 – 237NADP By similarity
Nucleotide binding55 – 573NADP By similarity
Nucleotide binding77 – 793NADP By similarity
Nucleotide binding117 – 1248NADP By similarity
Region31 – 366Substrate binding By similarity

Sites

Binding site111NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site711Substrate By similarity

Experimental info

Sequence conflict51K → L AA sequence Ref.1
Sequence conflict71N → D AA sequence Ref.1
Sequence conflict11 – 133AAC → IFD AA sequence Ref.1
Sequence conflict151N → D AA sequence Ref.1
Sequence conflict211N → D AA sequence Ref.1
Sequence conflict1581H → Q AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9U8B8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 9B8C0E50ED175812

FASTA18521,089
        10         20         30         40         50         60 
MSQVKLNLIA AACDNMGIGV NGALPWRLKK EMAYFTTMTS KVSEPTKVNA VIMGRRTWDC 

        70         80         90        100        110        120 
IPDKYRPLQD RVNIVLTHNV DSVKENVPEG VMVFPGLDEA IKYIEGREDI ESTWVIGGSS 

       130        140        150        160        170        180 
IYRAAMTHPN CGKIYLTEIQ KSFDCDTFFP NIDKQQFHLV DEEQIPGEKQ VEGNISYYFR 


VYKKL 

« Hide

References

[1]"Tobacco budworm dihydrofolate reductase is a promising target for insecticide discovery."
Walker V.K., Tyshenko M.G., Kuiper M.J., Dargar R.V., Yuhas D.A., Cruickshank P.A., Chaguturu R.
Eur. J. Biochem. 267:394-403(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 3-22; 32-38; 143-149; 153-159 AND 170-175, ENZYME REGULATION.
Tissue: Larva.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF104106 mRNA. Translation: AAF04459.1.

3D structure databases

ProteinModelPortalQ9U8B8.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00077; UER00158.

Family and domain databases

Gene3D3.40.430.10. 1 hit.
InterProIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSPR00070. DHFR.
SUPFAMSSF53597. SSF53597. 1 hit.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDYR_HELVI
AccessionPrimary (citable) accession number: Q9U8B8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: May 1, 2000
Last modified: October 16, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways